ID A0A0A2JLB0_PENEN Unreviewed; 318 AA.
AC A0A0A2JLB0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 13-SEP-2023, entry version 36.
DE RecName: Full=Proline iminopeptidase {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
DE Short=PIP {ECO:0000256|PIRNR:PIRNR006431};
DE EC=3.4.11.5 {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|PIRNR:PIRNR006431};
GN ORFNames=PEX2_057330 {ECO:0000313|EMBL:KGO53090.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO53090.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO53090.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO53090.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001585,
CC ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR006431}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088, ECO:0000256|PIRNR:PIRNR006431,
CC ECO:0000256|RuleBase:RU003421}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO53090.1}.
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DR EMBL; JQFZ01000252; KGO53090.1; -; Genomic_DNA.
DR RefSeq; XP_016595729.1; XM_016743007.1.
DR AlphaFoldDB; A0A0A2JLB0; -.
DR STRING; 27334.A0A0A2JLB0; -.
DR GeneID; 27678426; -.
DR HOGENOM; CLU_043739_2_2_1; -.
DR OrthoDB; 89932at2759; -.
DR PhylomeDB; A0A0A2JLB0; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0072330; P:monocarboxylic acid biosynthetic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR002410; Peptidase_S33.
DR InterPro; IPR005944; Pro_iminopeptidase.
DR NCBIfam; TIGR01249; pro_imino_pep_1; 1.
DR PANTHER; PTHR43722; PROLINE IMINOPEPTIDASE; 1.
DR PANTHER; PTHR43722:SF1; PROLINE IMINOPEPTIDASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF006431; Pept_S33; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|PIRNR:PIRNR006431,
KW ECO:0000256|RuleBase:RU003421}; Cytoplasm {ECO:0000256|PIRNR:PIRNR006431};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
KW Protease {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 38..295
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 265
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 293
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
SQ SEQUENCE 318 AA; 35860 MW; 6E42C3E9B0ACC45C CRC64;
MADLLTGYTH SAAFDIGRLL VSDIHTVHYE QYGKQDGKPI LYLHGGPGGH TSYNNTKYFN
PAIYRVVLFD QRGAGKSTPA AELRENTSQH LVSDIEVLRK HLQIAKWHVV FGGSWGSTLS
LLYAQAYPEM VGSLILRGIF TGRKSELEFS RGSIGAANIF PEAYEAFVNY LPEKDRARPN
EAYYDLLISE DYETRIAAAR EWNRWDLSIG TLRPDPEGFA QLEDDAWVLA HARLEAHYFA
NGVFLEEGQI LKEENLSTII QGRYDIVCAP QTAWDLHKGL PDSRLFWTPD AGHSATEPGT
QTKLFEVCDE YAELEFTH
//
